Header list of 1ien.pdb file
Complete list - 23 20 Bytes
HEADER TOXIN 10-APR-01 1IEN
TITLE SOLUTION STRUCTURE OF TIA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN TIA;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED. THIS SEQUENCE
SOURCE 4 OCCURS NATURALLY IN CONUS TULIPA (FISH-HUNTING CONE SNAIL).
KEYWDS CONOTOXIN, ALPHA1-ADRENOCEPTORS, TOXIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR I.A.SHARPE,J.GEHRMANN,M.L.LOUGHNAN,L.THOMAS,D.A.ADAMS,A.ATKINS,
AUTHOR 2 E.PALANT,D.J.CRAIK,D.J.ADAMS,P.F.ALEWOOD,R.J.LEWIS
REVDAT 3 23-FEB-22 1IEN 1 REMARK LINK
REVDAT 2 24-FEB-09 1IEN 1 VERSN
REVDAT 1 03-APR-02 1IEN 0
JRNL AUTH I.A.SHARPE,J.GEHRMANN,M.L.LOUGHNAN,L.THOMAS,D.A.ADAMS,
JRNL AUTH 2 A.ATKINS,E.PALANT,D.J.CRAIK,D.J.ADAMS,P.F.ALEWOOD,R.J.LEWIS
JRNL TITL TWO NEW CLASSES OF CONOPEPTIDES INHIBIT THE
JRNL TITL 2 ALPHA1-ADRENOCEPTOR AND NORADRENALINE TRANSPORTER.
JRNL REF NAT.NEUROSCI. V. 4 902 2001
JRNL REFN ISSN 1097-6256
JRNL PMID 11528421
JRNL DOI 10.1038/NN0901-902
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, X-PLOR 3.851
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON 213 DISTANCE RESTRAINTS DERIVED FROM
REMARK 3 17 INTRA-RESIDUE,
REMARK 3 93 SEQUENTIAL, 67 MEDIUM AND 36 LONG RANGE NOES, 7 DIHEDRAL AND 19
REMARK 3 ALPHA H CHEMICAL SHIFT RESTRAINTS.
REMARK 4
REMARK 4 1IEN COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-APR-01.
REMARK 100 THE DEPOSITION ID IS D_1000013213.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 285
REMARK 210 PH : 3.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2 MM TIA
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; DQF-COSY; E-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : ARX; AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX 230, X-PLOR 3.851
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : THE SUBMITTED CONFORMER MODELS
REMARK 210 ARE THE 20 STRUCTURES WITH THE
REMARK 210 LOWEST ENERGY.
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 4
REMARK 210
REMARK 210 REMARK: NULL
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 1 TRP A 3 CG - CD1 - NE1 ANGL. DEV. = -6.1 DEGREES
REMARK 500 1 TRP A 3 CD1 - NE1 - CE2 ANGL. DEV. = 7.5 DEGREES
REMARK 500 1 TRP A 3 NE1 - CE2 - CZ2 ANGL. DEV. = 7.0 DEGREES
REMARK 500 2 TRP A 3 CD1 - NE1 - CE2 ANGL. DEV. = 7.3 DEGREES
REMARK 500 2 TRP A 3 NE1 - CE2 - CZ2 ANGL. DEV. = 6.9 DEGREES
REMARK 500 3 TRP A 3 CD1 - NE1 - CE2 ANGL. DEV. = 7.4 DEGREES
REMARK 500 3 TRP A 3 NE1 - CE2 - CZ2 ANGL. DEV. = 7.1 DEGREES
REMARK 500 3 CYS A 19 CA - CB - SG ANGL. DEV. = 7.1 DEGREES
REMARK 500 4 TRP A 3 CG - CD1 - NE1 ANGL. DEV. = -6.0 DEGREES
REMARK 500 4 TRP A 3 CD1 - NE1 - CE2 ANGL. DEV. = 7.5 DEGREES
REMARK 500 4 TRP A 3 NE1 - CE2 - CZ2 ANGL. DEV. = 7.1 DEGREES
REMARK 500 5 TRP A 3 CG - CD1 - NE1 ANGL. DEV. = -6.0 DEGREES
REMARK 500 5 TRP A 3 CD1 - NE1 - CE2 ANGL. DEV. = 7.4 DEGREES
REMARK 500 5 TRP A 3 NE1 - CE2 - CZ2 ANGL. DEV. = 7.0 DEGREES
REMARK 500 6 TRP A 3 CD1 - NE1 - CE2 ANGL. DEV. = 7.4 DEGREES
REMARK 500 6 TRP A 3 NE1 - CE2 - CZ2 ANGL. DEV. = 7.1 DEGREES
REMARK 500 6 CYS A 6 CA - CB - SG ANGL. DEV. = 7.8 DEGREES
REMARK 500 7 TRP A 3 CD1 - NE1 - CE2 ANGL. DEV. = 7.4 DEGREES
REMARK 500 7 TRP A 3 NE1 - CE2 - CZ2 ANGL. DEV. = 7.1 DEGREES
REMARK 500 7 CYS A 6 CA - CB - SG ANGL. DEV. = 7.6 DEGREES
REMARK 500 8 TRP A 3 CG - CD1 - NE1 ANGL. DEV. = -6.2 DEGREES
REMARK 500 8 TRP A 3 CD1 - NE1 - CE2 ANGL. DEV. = 7.3 DEGREES
REMARK 500 8 TRP A 3 NE1 - CE2 - CZ2 ANGL. DEV. = 7.1 DEGREES
REMARK 500 9 TRP A 3 CD1 - NE1 - CE2 ANGL. DEV. = 7.3 DEGREES
REMARK 500 9 TRP A 3 NE1 - CE2 - CZ2 ANGL. DEV. = 7.0 DEGREES
REMARK 500 10 TRP A 3 CD1 - NE1 - CE2 ANGL. DEV. = 7.3 DEGREES
REMARK 500 10 TRP A 3 NE1 - CE2 - CZ2 ANGL. DEV. = 6.9 DEGREES
REMARK 500 11 TRP A 3 CD1 - NE1 - CE2 ANGL. DEV. = 7.3 DEGREES
REMARK 500 11 TRP A 3 NE1 - CE2 - CZ2 ANGL. DEV. = 6.9 DEGREES
REMARK 500 11 ARG A 12 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 12 TRP A 3 CG - CD1 - NE1 ANGL. DEV. = -6.1 DEGREES
REMARK 500 12 TRP A 3 CD1 - NE1 - CE2 ANGL. DEV. = 7.4 DEGREES
REMARK 500 12 TRP A 3 NE1 - CE2 - CZ2 ANGL. DEV. = 7.0 DEGREES
REMARK 500 13 TRP A 3 CD1 - NE1 - CE2 ANGL. DEV. = 7.2 DEGREES
REMARK 500 14 TRP A 3 CG - CD1 - NE1 ANGL. DEV. = -6.0 DEGREES
REMARK 500 14 TRP A 3 CD1 - NE1 - CE2 ANGL. DEV. = 7.4 DEGREES
REMARK 500 14 TRP A 3 NE1 - CE2 - CZ2 ANGL. DEV. = 7.1 DEGREES
REMARK 500 15 TRP A 3 CG - CD1 - NE1 ANGL. DEV. = -6.0 DEGREES
REMARK 500 15 TRP A 3 CD1 - NE1 - CE2 ANGL. DEV. = 7.4 DEGREES
REMARK 500 15 TRP A 3 NE1 - CE2 - CZ2 ANGL. DEV. = 7.1 DEGREES
REMARK 500 16 TRP A 3 CD1 - NE1 - CE2 ANGL. DEV. = 7.4 DEGREES
REMARK 500 16 TRP A 3 NE1 - CE2 - CZ2 ANGL. DEV. = 7.0 DEGREES
REMARK 500 17 TRP A 3 CG - CD1 - NE1 ANGL. DEV. = -6.0 DEGREES
REMARK 500 17 TRP A 3 CD1 - NE1 - CE2 ANGL. DEV. = 7.3 DEGREES
REMARK 500 17 TRP A 3 NE1 - CE2 - CZ2 ANGL. DEV. = 7.0 DEGREES
REMARK 500 18 TRP A 3 CG - CD1 - NE1 ANGL. DEV. = -6.1 DEGREES
REMARK 500 18 TRP A 3 CD1 - NE1 - CE2 ANGL. DEV. = 7.4 DEGREES
REMARK 500 18 TRP A 3 NE1 - CE2 - CZ2 ANGL. DEV. = 7.0 DEGREES
REMARK 500 19 TRP A 3 CG - CD1 - NE1 ANGL. DEV. = -6.0 DEGREES
REMARK 500 19 TRP A 3 CD1 - NE1 - CE2 ANGL. DEV. = 7.3 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 54 ANGLE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 1 ASN A 2 -146.05 51.50
REMARK 500 2 ASN A 2 -148.75 56.18
REMARK 500 2 LYS A 16 -77.39 -52.97
REMARK 500 3 ASN A 2 -144.39 53.82
REMARK 500 3 HIS A 15 -54.06 -140.91
REMARK 500 3 LYS A 16 -6.82 64.45
REMARK 500 4 ASN A 2 -142.65 49.35
REMARK 500 4 HIS A 15 48.63 -140.12
REMARK 500 4 LYS A 16 -78.65 -61.04
REMARK 500 5 ASN A 2 -143.50 50.99
REMARK 500 5 HIS A 15 -59.97 -131.65
REMARK 500 5 LYS A 16 -56.47 74.66
REMARK 500 6 ASN A 2 -141.33 46.01
REMARK 500 6 HIS A 15 28.85 -150.49
REMARK 500 6 LYS A 16 -64.44 -15.33
REMARK 500 7 ASN A 2 -146.13 52.96
REMARK 500 7 LYS A 16 -78.41 -34.39
REMARK 500 8 ASN A 2 -139.37 37.30
REMARK 500 8 LYS A 16 -89.88 -55.37
REMARK 500 9 ASN A 2 -150.96 57.24
REMARK 500 9 HIS A 15 -78.38 -144.54
REMARK 500 9 LYS A 16 -39.38 73.54
REMARK 500 10 ASN A 2 -144.47 51.63
REMARK 500 10 ALA A 10 -6.98 -58.85
REMARK 500 10 LYS A 16 -39.21 -26.23
REMARK 500 11 ASN A 2 -143.51 53.43
REMARK 500 12 ASN A 2 -148.68 55.05
REMARK 500 12 CYS A 6 -8.94 -59.08
REMARK 500 12 HIS A 15 -66.70 -101.33
REMARK 500 12 LYS A 16 -60.68 78.27
REMARK 500 13 ASN A 2 -151.53 58.10
REMARK 500 13 LYS A 16 -72.86 -58.52
REMARK 500 14 ASN A 2 -145.61 50.51
REMARK 500 14 HIS A 15 36.33 -144.89
REMARK 500 14 LYS A 16 -71.75 -57.72
REMARK 500 15 ASN A 2 -142.52 50.79
REMARK 500 15 ALA A 10 5.74 -68.88
REMARK 500 15 CYS A 11 -51.18 -123.01
REMARK 500 15 HIS A 15 -71.35 -136.60
REMARK 500 15 LYS A 16 -58.52 75.53
REMARK 500 16 ASN A 2 -146.16 54.96
REMARK 500 17 ASN A 2 -147.34 50.07
REMARK 500 17 HIS A 15 -76.23 -90.56
REMARK 500 17 LYS A 16 -7.90 66.09
REMARK 500 17 LYS A 17 -19.22 -140.21
REMARK 500 18 ASN A 2 -156.81 54.13
REMARK 500 19 ASN A 2 -154.86 53.52
REMARK 500 19 HIS A 15 49.79 -143.60
REMARK 500 19 LYS A 16 -80.28 -58.46
REMARK 500 20 ASN A 2 -140.05 50.81
REMARK 500
REMARK 500 THIS ENTRY HAS 51 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH2 A 20
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1IEO RELATED DB: PDB
REMARK 900 1IEO SEQUENCE (SYNTHETIC) OF CONUS MARMOREUS (MOLLUSC-HUNTING CONE
REMARK 900 SNAIL)
DBREF 1IEN A 1 19 UNP P58811 CXR_CONTU 1 19
SEQRES 1 A 20 PHE ASN TRP ARG CYS CYS LEU ILE PRO ALA CYS ARG ARG
SEQRES 2 A 20 ASN HIS LYS LYS PHE CYS NH2
HET NH2 A 20 3
HETNAM NH2 AMINO GROUP
FORMUL 1 NH2 H2 N
HELIX 1 1 TRP A 3 ILE A 8 1 6
HELIX 2 2 ILE A 8 ARG A 13 1 6
HELIX 3 3 HIS A 15 CYS A 19 5 5
SSBOND 1 CYS A 5 CYS A 11 1555 1555 2.02
SSBOND 2 CYS A 6 CYS A 19 1555 1555 2.02
LINK C CYS A 19 N NH2 A 20 1555 1555 1.31
SITE 1 AC1 2 LYS A 16 CYS A 19
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
Complete list - 23 20 Bytes